Structural Studies of a Bacterial Condensin Complex Reveal ATP-Dependent Disruption of Intersubunit Interactions

@article{Woo2009StructuralSO,
  title={Structural Studies of a Bacterial Condensin Complex Reveal ATP-Dependent Disruption of Intersubunit Interactions},
  author={Jae-Sung Woo and Jae-Hong Lim and Ho-Chul Shin and Min-Kang Suh and B. Ku and Kwang-Hoon Lee and K. Joo and H. Robinson and J. Lee and S. Park and N. Ha and B. Oh},
  journal={Cell},
  year={2009},
  volume={136},
  pages={85-96}
}
  • Jae-Sung Woo, Jae-Hong Lim, +9 authors B. Oh
  • Published 2009
  • Biology, Medicine
  • Cell
    • Condensins are key mediators of chromosome condensation across organisms. Like other condensins, the bacterial MukBEF condensin complex consists of an SMC family protein dimer containing two ATPase head domains, MukB, and two interacting subunits, MukE and MukF. We report complete structural views of the intersubunit interactions of this condensin along with ensuing studies that reveal a role for the ATPase activity of MukB. MukE and MukF together form an elongated dimeric frame, and MukF's C… CONTINUE READING
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